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Closed-gate KcsA soaked in 0mM KCl/5mM BaCl2Closed-gate KcsA soaked in 0mM KCl/5mM BaCl2
Structural highlights
FunctionKCSA_STRLI Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).[1] Publication Abstract from PubMedBarium (Ba(2+)) is a classic permeant blocker of potassium (K(+)) channels. The "external lock-in effect" in barium block experiments, whereby the binding of external K(+) impedes the forward translocation of the blocker, provides a powerful avenue to investigate the selectivity of the binding sites along the pore of potassium channels. Barium block experiments show that the external lock-in site is highly selective for K(+) over Na(+). Wild-type KcsA was crystallized in low K(+) conditions, and the crystals were soaked in solutions containing various concentrations of barium. Structural analysis reveals open and closed gate conformations of the KcsA channel. Anomalous diffraction experiments show that Ba(2+) primarily binds to the innermost site S4 of the selectivity filter of the open-gate conformation and also the site S2, but no binding is detected with the closed-gate conformation. Alchemical free-energy perturbation calculations indicate that the presence of a Ba(2+) ion in the selectivity filter boosts the specificity of K(+) binding relative to Na(+) in the external sites S0-S2. Open and Closed Structures of a Barium-Blocked Potassium Channel.,Rohaim A, Gong L, Li J, Rui H, Blachowicz L, Roux B J Mol Biol. 2020 Aug 7;432(17):4783-4798. doi: 10.1016/j.jmb.2020.06.012. Epub, 2020 Jun 29. PMID:32615129[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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